Výsledky vyhledávání - "Jeff D. Ballin"

Developmental and reproductive safety evaluation of AV7909 anthrax vaccine candidate in rats

Autor: Jeffry D. Shearer, Bruna Blauth, Jeff D Ballin, Eve Mylchreest, Joshua J. Reece, M. Autumn Smiley, Boris Ionin, Vladimir Savransky

Publikováno v: Birth Defects Research

The AV7909 vaccine, consists of the Anthrax Vaccine Adsorbed (AVA) bulk drug substance and the immunostimulatory Toll‐like receptor 9 agonist oligodeoxynucleotide adjuvant CPG 7909. The purpose of this research was to evaluate the potential materna

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98c1f2df5891f439f40def74e567bacf
https://pubmed.ncbi.nlm.nih.gov/33067910

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Fluorescence intensity decays of 2-aminopurine solutions: Lifetime distribution approach

Autor: Pabak Sarkar, Gerald M. Wilson, Shashank Bharill, Zygmunt Gryczynski, Jeff D. Ballin, Ignacy Gryczynski

Publikováno v: Analytical Biochemistry. 377:141-149

The fluorescent adenine analogue 2-aminopurine (2AP) has been used extensively to monitor conformational changes and macromolecular binding events involving nucleic acids because its fluorescence properties are highly sensitive to changes in chemical

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0bbc252d99641fce1c55dd4576d14a82
https://doi.org/10.1016/j.ab.2008.03.034

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Site-Specific Variations in RNA Folding Thermodynamics Visualized by 2-Aminopurine Fluorescence

Autor: Gerald M. Wilson, Jeff D. Ballin, Elizabeth J. Fialcowitz-White, Zygmunt Gryczynski, Shashank Bharill, Ignacy Gryczynski

Publikováno v: Biochemistry. 46:13948-13960

The fluorescent base analogue 2-aminopurine (2-AP) is commonly used to study specific conformational and protein binding events involving nucleic acids. Here, combinations of steady-state and time-resolved fluorescence spectroscopy of 2-AP were emplo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9156894ba402304b92f55a84f3ca1fc8
https://doi.org/10.1021/bi7011977

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Substrate Dependence of Conformational Changes in the RNA-Binding Domain of Tristetraprolin Assessed by Fluorescence Spectroscopy of Tryptophan Mutants

Autor: Elizabeth J. Fialcowitz-White, Perry J. Blackshear, Gerald M. Wilson, Brandy Y. Brewer, Jeff D. Ballin

Publikováno v: Biochemistry. 45:13807-13817

Association of tristetraprolin (TTP) with mRNAs containing selected AU-rich mRNA-destabilizing elements (AREs) initiates rapid cytoplasmic degradation of these transcripts. The RNA-binding activity of TTP is mediated by an internal tandem zinc finger

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd4f102c0e47ba7edd9b581c42180fd8
https://doi.org/10.1021/bi061320j

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Interactions of the KWK6 cationic peptide with short nucleic acid oligomers: demonstration of large Coulombic end effects on binding at 0.1-0.2 M salt

Autor: Irina A. Shkel, Jeff D. Ballin, M. Thomas Record

Publikováno v: Nucleic Acids Research. 32:3271-3281

We quantify Coulombic end effects (CEE) on oligocation-nucleic acid interactions at salt concentrations ([salt]) in the physiological range. Binding constants (K(obs); per site, at zero binding density) for the +8-charged C-amidated oligopeptide KWK6

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95f4061791207964124a1cfe31007dc2
https://doi.org/10.1093/nar/gkh646

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HNO enhances SERCA2a activity and cardiomyocyte function by promoting redox-dependent phospholamban oligomerization

Autor: David A. Kass, Vidhya Sivakumaran, Lufang Zhou, Sabine Huke, Brian O'Rourke, Dong I. Lee, Brian A. Stanley, Carlo G. Tocchetti, James E. Mahaney, John P. Toscano, Peter P. Rainer, Evangelia G. Kranias, Gizem Keceli, Viviane Caceres, Jeff D. Ballin, Mark T. Ziolo, Nazareno Paolocci, Gerald M. Wilson

Publikováno v: Antioxidantsredox signaling. 19(11)

Aims: Nitroxyl (HNO) interacts with thiols to act as a redox-sensitive modulator of protein function. It enhances sarcoplasmic reticular Ca2+ uptake and myofilament Ca2+ sensitivity, improving cardiac contractility. This activity has led to clinical

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0144274de795a130b1a076238fca2591
https://pubmed.ncbi.nlm.nih.gov/23919584

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Role and Applications of Electrostatic Effects on Nucleic Acid Conformational Transitions and Binding Processes

Autor: Jeff D. Ballin, Gerald M. Wilson

Publikováno v: Application of Thermodynamics to Biological and Materials Science

Processes involving nucleic acids are in general highly salt concentration dependent. Equilibrium binding constants (Kobs, defined in terms of the concentrations of the reactants and products) describing the association of proteins or multivalent lig

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e50dc75259c0d9cc859f0db71cf54416
http://www.intechopen.com/articles/show/title/role-and-applications-of-electrostatic-effects-on-nucleic-acid-conformational-transitions-and-bindin

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Unique properties of the Mtr4p-poly(A) complex suggest a role in substrate targeting†

Autor: Eric A. Toth, Jeff D. Ballin, Gerald M. Wilson, Dimeka N. Patterson, Jade Bernstein

Mtr4p is a DEVH-box helicase required for 3'-end processing and degradation of various nuclear RNA substrates. In particular, Mtr4p is essential for the creation of 5.8S rRNA, U4 snRNA, and some snoRNAs and for the degradation of cryptic unstable tra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72566346b3caa47cddb43f7a8053edca
https://europepmc.org/articles/PMC2999651/

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Alternatively Expressed Domains of AU-rich Element RNA-binding Protein 1 (AUF1) Regulate RNA-binding Affinity, RNA-induced Protein Oligomerization, and the Local Conformation of Bound RNA Ligands*

Autor: Eric A. Toth, Christina R. Ross, Jun Huang, Jeff D. Ballin, Brandy Y. Brewer, Beth E. Zucconi, Gerald M. Wilson

AU-rich element RNA-binding protein 1 (AUF1) binding to AU-rich elements (AREs) in the 3′-untranslated regions of mRNAs encoding many cytokines and other regulatory proteins modulates mRNA stability, thereby influencing protein expression. AUF1-mRN

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::408312950e288d715a5370ba79dc8a63
https://europepmc.org/articles/PMC2998080/

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Contributions of the histidine side chain and the N-terminal alpha-amino group to the binding thermodynamics of oligopeptides to nucleic acids as a function of pH

Autor: James P. Prevas, Gerald M. Wilson, Jeff D. Ballin, M. Thomas Record, Christina R. Ross, Eric A. Toth

Publikováno v: Biochemistry. 49(9)

Interactions of histidine with nucleic acid phosphates and histidine pK(a) shifts make important contributions to many protein-nucleic acid binding processes. To characterize these phenomena in simplified systems, we quantified binding of a histidine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5300fab02dfbb3eb9d2e1df4271b24f0
https://pubmed.ncbi.nlm.nih.gov/20108951

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